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Protein

Chondroitin sulfate proteoglycan 4

Gene

CSPG4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades.3 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Transducer

Keywords - Biological processi

Angiogenesis, Differentiation, Tissue remodeling

Enzyme and pathway databases

ReactomeiR-HSA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-HSA-2022870. Chondroitin sulfate biosynthesis.
R-HSA-2022923. Dermatan sulfate biosynthesis.
R-HSA-2024101. CS/DS degradation.
R-HSA-3560783. Defective B4GALT7 causes EDS, progeroid type.
R-HSA-3560801. Defective B3GAT3 causes JDSSDHD.
R-HSA-3595172. Defective CHST3 causes SEDCJD.
R-HSA-3595174. Defective CHST14 causes EDS, musculocontractural type.
R-HSA-3595177. Defective CHSY1 causes TPBS.
R-HSA-4420332. Defective B3GALT6 causes EDSP2 and SEMDJL1.
SignaLinkiQ6UVK1.

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin sulfate proteoglycan 4
Alternative name(s):
Chondroitin sulfate proteoglycan NG2
Melanoma chondroitin sulfate proteoglycan
Melanoma-associated chondroitin sulfate proteoglycan
Gene namesi
Name:CSPG4
Synonyms:MCSP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:2466. CSPG4.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity; Extracellular side By similarity
  • Apical cell membrane By similarity; Single-pass type I membrane protein By similarity; Extracellular side By similarity
  • Cell projectionlamellipodium membrane By similarity; Single-pass type I membrane protein By similarity; Extracellular side By similarity
  • Cell surface By similarity

  • Note: Localized at the apical plasma membrane it relocalizes to the lamellipodia of astrocytoma upon phosphorylation by PRKCA. Localizes to the retraction fibers. Localizes to the plasma membrane of oligodendrocytes (By similarity).By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini30 – 2224ExtracellularBy similarityAdd BLAST2195
Transmembranei2225 – 2245HelicalSequence analysisAdd BLAST21
Topological domaini2246 – 2322CytoplasmicBy similarityAdd BLAST77

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • focal adhesion Source: UniProtKB
  • Golgi lumen Source: Reactome
  • integral component of plasma membrane Source: ProtInc
  • lamellipodium membrane Source: UniProtKB-SubCell
  • lysosomal lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi1464.
OpenTargetsiENSG00000173546.
PharmGKBiPA26963.

Polymorphism and mutation databases

BioMutaiCSPG4.
DMDMi296434468.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000004196230 – 2322Chondroitin sulfate proteoglycan 4Add BLAST2293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi130N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi169 ↔ 192PROSITE-ProRule annotation
Glycosylationi348N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi354 ↔ 380PROSITE-ProRule annotation
Glycosylationi427N-linked (GlcNAc...)Sequence analysis1
Glycosylationi685N-linked (GlcNAc...)Sequence analysis1
Glycosylationi772N-linked (GlcNAc...)Sequence analysis1
Glycosylationi995O-linked (Xyl...) (chondroitin sulfate)By similarity1
Glycosylationi1131N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1202N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1364N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1449N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1645N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1909N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2016N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2034N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2040N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2075N-linked (GlcNAc...)1 Publication1
Modified residuei2252Phosphothreonine; by PKC/PRKCABy similarity1

Post-translational modificationi

O-glycosylated; contains glycosaminoglycan chondroitin sulfate which are required for proper localization and function in stress fiber formation (By similarity). Involved in interaction with MMP16 and ITGA4.By similarity1 Publication
Phosphorylation by PRKCA regulates its subcellular location and function in cell motility.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

EPDiQ6UVK1.
MaxQBiQ6UVK1.
PaxDbiQ6UVK1.
PeptideAtlasiQ6UVK1.
PRIDEiQ6UVK1.

PTM databases

iPTMnetiQ6UVK1.
PhosphoSitePlusiQ6UVK1.

Expressioni

Tissue specificityi

Detected only in malignant melanoma cells.1 Publication

Gene expression databases

BgeeiENSG00000173546.
CleanExiHS_CSPG4.
GenevisibleiQ6UVK1. HS.

Organism-specific databases

HPAiCAB016189.
HPA002951.
HPA042785.

Interactioni

Subunit structurei

Interacts with the first PDZ domain of MPDZ. Interacts with PRKCA. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and angiostatin. Binds FGF2 and PDGFA. Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and GRIA2 (By similarity). Interacts with LGALS3 and the integrin composed of ITGB1 and ITGA3. Interacts with ITGA4 through its chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1. Interacts with MMP16.By similarity4 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107846. 12 interactors.
IntActiQ6UVK1. 14 interactors.
MINTiMINT-1197576.
STRINGi9606.ENSP00000312506.

Structurei

3D structure databases

ProteinModelPortaliQ6UVK1.
SMRiQ6UVK1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 192Laminin G-like 1PROSITE-ProRule annotationAdd BLAST163
Domaini202 – 380Laminin G-like 2PROSITE-ProRule annotationAdd BLAST179
Repeati430 – 523CSPG 11 PublicationAdd BLAST94
Repeati556 – 643CSPG 21 PublicationAdd BLAST88
Repeati665 – 764CSPG 31 PublicationAdd BLAST100
Repeati792 – 878CSPG 41 PublicationAdd BLAST87
Repeati900 – 989CSPG 51 PublicationAdd BLAST90
Repeati1020 – 1108CSPG 61 PublicationAdd BLAST89
Repeati1128 – 1216CSPG 71 PublicationAdd BLAST89
Repeati1241 – 1337CSPG 81 PublicationAdd BLAST97
Repeati1360 – 1449CSPG 91 PublicationAdd BLAST90
Repeati1476 – 1561CSPG 101 PublicationAdd BLAST86
Repeati1583 – 1679CSPG 111 PublicationAdd BLAST97
Repeati1707 – 1803CSPG 121 PublicationAdd BLAST97
Repeati1835 – 1922CSPG 131 PublicationAdd BLAST88
Repeati1944 – 2029CSPG 141 PublicationAdd BLAST86
Repeati2048 – 2147CSPG 151 PublicationAdd BLAST100

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 639Globular or compact configuration stabilized by disulfide bondsAdd BLAST610
Regioni30 – 639Neurite growth inhibitionBy similarityAdd BLAST610
Regioni574 – 1040Interaction with COL6A2By similarityAdd BLAST467
Regioni631 – 1446Interaction with COL5A1By similarityAdd BLAST816
Regioni1586 – 2221Neurite growth inhibitionBy similarityAdd BLAST636
Regioni1587 – 2221Cysteine-containingAdd BLAST635

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2320 – 2322PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi639 – 1586Gly/Ser-rich (glycosaminoglycan attachment domain)Add BLAST948

Sequence similaritiesi

Contains 15 CSPG (NG2) repeats.Curated
Contains 2 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3597. Eukaryota.
ENOG410XQ29. LUCA.
GeneTreeiENSGT00550000074429.
HOGENOMiHOG000170195.
HOVERGENiHBG081360.
InParanoidiQ6UVK1.
KOiK08115.
OMAiRPIYRFT.
OrthoDBiEOG091G00BN.
PhylomeDBiQ6UVK1.
TreeFamiTF316876.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
SMARTiSM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6UVK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSGPRPPLP APGLALALTL TMLARLASAA SFFGENHLEV PVATALTDID
60 70 80 90 100
LQLQFSTSQP EALLLLAAGP ADHLLLQLYS GRLQVRLVLG QEELRLQTPA
110 120 130 140 150
ETLLSDSIPH TVVLTVVEGW ATLSVDGFLN ASSAVPGAPL EVPYGLFVGG
160 170 180 190 200
TGTLGLPYLR GTSRPLRGCL HAATLNGRSL LRPLTPDVHE GCAEEFSASD
210 220 230 240 250
DVALGFSGPH SLAAFPAWGT QDEGTLEFTL TTQSRQAPLA FQAGGRRGDF
260 270 280 290 300
IYVDIFEGHL RAVVEKGQGT VLLHNSVPVA DGQPHEVSVH INAHRLEISV
310 320 330 340 350
DQYPTHTSNR GVLSYLEPRG SLLLGGLDAE ASRHLQEHRL GLTPEATNAS
360 370 380 390 400
LLGCMEDLSV NGQRRGLREA LLTRNMAAGC RLEEEEYEDD AYGHYEAFST
410 420 430 440 450
LAPEAWPAME LPEPCVPEPG LPPVFANFTQ LLTISPLVVA EGGTAWLEWR
460 470 480 490 500
HVQPTLDLME AELRKSQVLF SVTRGARHGE LELDIPGAQA RKMFTLLDVV
510 520 530 540 550
NRKARFIHDG SEDTSDQLVL EVSVTARVPM PSCLRRGQTY LLPIQVNPVN
560 570 580 590 600
DPPHIIFPHG SLMVILEHTQ KPLGPEVFQA YDPDSACEGL TFQVLGTSSG
610 620 630 640 650
LPVERRDQPG EPATEFSCRE LEAGSLVYVH RGGPAQDLTF RVSDGLQASP
660 670 680 690 700
PATLKVVAIR PAIQIHRSTG LRLAQGSAMP ILPANLSVET NAVGQDVSVL
710 720 730 740 750
FRVTGALQFG ELQKQGAGGV EGAEWWATQA FHQRDVEQGR VRYLSTDPQH
760 770 780 790 800
HAYDTVENLA LEVQVGQEIL SNLSFPVTIQ RATVWMLRLE PLHTQNTQQE
810 820 830 840 850
TLTTAHLEAT LEEAGPSPPT FHYEVVQAPR KGNLQLQGTR LSDGQGFTQD
860 870 880 890 900
DIQAGRVTYG ATARASEAVE DTFRFRVTAP PYFSPLYTFP IHIGGDPDAP
910 920 930 940 950
VLTNVLLVVP EGGEGVLSAD HLFVKSLNSA SYLYEVMERP RHGRLAWRGT
960 970 980 990 1000
QDKTTMVTSF TNEDLLRGRL VYQHDDSETT EDDIPFVATR QGESSGDMAW
1010 1020 1030 1040 1050
EEVRGVFRVA IQPVNDHAPV QTISRIFHVA RGGRRLLTTD DVAFSDADSG
1060 1070 1080 1090 1100
FADAQLVLTR KDLLFGSIVA VDEPTRPIYR FTQEDLRKRR VLFVHSGADR
1110 1120 1130 1140 1150
GWIQLQVSDG QHQATALLEV QASEPYLRVA NGSSLVVPQG GQGTIDTAVL
1160 1170 1180 1190 1200
HLDTNLDIRS GDEVHYHVTA GPRWGQLVRA GQPATAFSQQ DLLDGAVLYS
1210 1220 1230 1240 1250
HNGSLSPRDT MAFSVEAGPV HTDATLQVTI ALEGPLAPLK LVRHKKIYVF
1260 1270 1280 1290 1300
QGEAAEIRRD QLEAAQEAVP PADIVFSVKS PPSAGYLVMV SRGALADEPP
1310 1320 1330 1340 1350
SLDPVQSFSQ EAVDTGRVLY LHSRPEAWSD AFSLDVASGL GAPLEGVLVE
1360 1370 1380 1390 1400
LEVLPAAIPL EAQNFSVPEG GSLTLAPPLL RVSGPYFPTL LGLSLQVLEP
1410 1420 1430 1440 1450
PQHGALQKED GPQARTLSAF SWRMVEEQLI RYVHDGSETL TDSFVLMANA
1460 1470 1480 1490 1500
SEMDRQSHPV AFTVTVLPVN DQPPILTTNT GLQMWEGATA PIPAEALRST
1510 1520 1530 1540 1550
DGDSGSEDLV YTIEQPSNGR VVLRGAPGTE VRSFTQAQLD GGLVLFSHRG
1560 1570 1580 1590 1600
TLDGGFRFRL SDGEHTSPGH FFRVTAQKQV LLSLKGSQTL TVCPGSVQPL
1610 1620 1630 1640 1650
SSQTLRASSS AGTDPQLLLY RVVRGPQLGR LFHAQQDSTG EALVNFTQAE
1660 1670 1680 1690 1700
VYAGNILYEH EMPPEPFWEA HDTLELQLSS PPARDVAATL AVAVSFEAAC
1710 1720 1730 1740 1750
PQRPSHLWKN KGLWVPEGQR ARITVAALDA SNLLASVPSP QRSEHDVLFQ
1760 1770 1780 1790 1800
VTQFPSRGQL LVSEEPLHAG QPHFLQSQLA AGQLVYAHGG GGTQQDGFHF
1810 1820 1830 1840 1850
RAHLQGPAGA SVAGPQTSEA FAITVRDVNE RPPQPQASVP LRLTRGSRAP
1860 1870 1880 1890 1900
ISRAQLSVVD PDSAPGEIEY EVQRAPHNGF LSLVGGGLGP VTRFTQADVD
1910 1920 1930 1940 1950
SGRLAFVANG SSVAGIFQLS MSDGASPPLP MSLAVDILPS AIEVQLRAPL
1960 1970 1980 1990 2000
EVPQALGRSS LSQQQLRVVS DREEPEAAYR LIQGPQYGHL LVGGRPTSAF
2010 2020 2030 2040 2050
SQFQIDQGEV VFAFTNFSSS HDHFRVLALA RGVNASAVVN VTVRALLHVW
2060 2070 2080 2090 2100
AGGPWPQGAT LRLDPTVLDA GELANRTGSV PRFRLLEGPR HGRVVRVPRA
2110 2120 2130 2140 2150
RTEPGGSQLV EQFTQQDLED GRLGLEVGRP EGRAPGPAGD SLTLELWAQG
2160 2170 2180 2190 2200
VPPAVASLDF ATEPYNAARP YSVALLSVPE AARTEAGKPE SSTPTGEPGP
2210 2220 2230 2240 2250
MASSPEPAVA KGGFLSFLEA NMFSVIIPMC LVLLLLALIL PLLFYLRKRN
2260 2270 2280 2290 2300
KTGKHDVQVL TAKPRNGLAG DTETFRKVEP GQAIPLTAVP GQGPPPGGQP
2310 2320
DPELLQFCRT PNPALKNGQY WV
Length:2,322
Mass (Da):250,537
Last modified:May 18, 2010 - v2
Checksum:i0B4F39AFC5ADD3CA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5 – 6PR → RG in CAA65529 (PubMed:8790396).Curated2
Sequence conflicti5 – 6PR → RG in AAQ62842 (PubMed:15210734).Curated2
Sequence conflicti477 – 478RH → HY in CAA65529 (PubMed:8790396).Curated2
Sequence conflicti486P → L in CAA65529 (PubMed:8790396).Curated1
Sequence conflicti631R → C in CAA65529 (PubMed:8790396).Curated1
Sequence conflicti715 – 717QGA → HST in CAA65529 (PubMed:8790396).Curated3
Sequence conflicti942H → L in CAA65529 (PubMed:8790396).Curated1
Sequence conflicti1208R → E in CAA65529 (PubMed:8790396).Curated1
Sequence conflicti1405A → P in CAA65529 (PubMed:8790396).Curated1
Sequence conflicti1557R → P in CAA65529 (PubMed:8790396).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0617331703R → H.Corresponds to variant rs8023621dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96753 mRNA. Translation: CAA65529.1.
AY359468 mRNA. Translation: AAQ62842.1.
AC105020 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99239.1.
CH471136 Genomic DNA. Translation: EAW99240.1.
CCDSiCCDS10284.1.
RefSeqiNP_001888.2. NM_001897.4.
UniGeneiHs.513044.

Genome annotation databases

EnsembliENST00000308508; ENSP00000312506; ENSG00000173546.
GeneIDi1464.
KEGGihsa:1464.
UCSCiuc002baw.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96753 mRNA. Translation: CAA65529.1.
AY359468 mRNA. Translation: AAQ62842.1.
AC105020 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99239.1.
CH471136 Genomic DNA. Translation: EAW99240.1.
CCDSiCCDS10284.1.
RefSeqiNP_001888.2. NM_001897.4.
UniGeneiHs.513044.

3D structure databases

ProteinModelPortaliQ6UVK1.
SMRiQ6UVK1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107846. 12 interactors.
IntActiQ6UVK1. 14 interactors.
MINTiMINT-1197576.
STRINGi9606.ENSP00000312506.

PTM databases

iPTMnetiQ6UVK1.
PhosphoSitePlusiQ6UVK1.

Polymorphism and mutation databases

BioMutaiCSPG4.
DMDMi296434468.

Proteomic databases

EPDiQ6UVK1.
MaxQBiQ6UVK1.
PaxDbiQ6UVK1.
PeptideAtlasiQ6UVK1.
PRIDEiQ6UVK1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308508; ENSP00000312506; ENSG00000173546.
GeneIDi1464.
KEGGihsa:1464.
UCSCiuc002baw.3. human.

Organism-specific databases

CTDi1464.
DisGeNETi1464.
GeneCardsiCSPG4.
H-InvDBHIX0026925.
HIX0038117.
HIX0172852.
HIX0177623.
HIX0177624.
HGNCiHGNC:2466. CSPG4.
HPAiCAB016189.
HPA002951.
HPA042785.
MIMi601172. gene.
neXtProtiNX_Q6UVK1.
OpenTargetsiENSG00000173546.
PharmGKBiPA26963.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3597. Eukaryota.
ENOG410XQ29. LUCA.
GeneTreeiENSGT00550000074429.
HOGENOMiHOG000170195.
HOVERGENiHBG081360.
InParanoidiQ6UVK1.
KOiK08115.
OMAiRPIYRFT.
OrthoDBiEOG091G00BN.
PhylomeDBiQ6UVK1.
TreeFamiTF316876.

Enzyme and pathway databases

ReactomeiR-HSA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-HSA-2022870. Chondroitin sulfate biosynthesis.
R-HSA-2022923. Dermatan sulfate biosynthesis.
R-HSA-2024101. CS/DS degradation.
R-HSA-3560783. Defective B4GALT7 causes EDS, progeroid type.
R-HSA-3560801. Defective B3GAT3 causes JDSSDHD.
R-HSA-3595172. Defective CHST3 causes SEDCJD.
R-HSA-3595174. Defective CHST14 causes EDS, musculocontractural type.
R-HSA-3595177. Defective CHSY1 causes TPBS.
R-HSA-4420332. Defective B3GALT6 causes EDSP2 and SEMDJL1.
SignaLinkiQ6UVK1.

Miscellaneous databases

ChiTaRSiCSPG4. human.
GeneWikiiCSPG4.
GenomeRNAii1464.
PROiQ6UVK1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173546.
CleanExiHS_CSPG4.
GenevisibleiQ6UVK1. HS.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
SMARTiSM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCSPG4_HUMAN
AccessioniPrimary (citable) accession number: Q6UVK1
Secondary accession number(s): D3DW77, Q92675
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: May 18, 2010
Last modified: November 2, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Valuable marker for several incompletely differentiated precursor cells.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.